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The crystal structure of encm L144M mutant complex with dioxygen under 15 bars O2 pressure

Analyse The crystal structure of encm L144M mutant complex with dioxygen under 15 bars… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6FYC
Type: protein
Length: 906 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative FAD-dependent oxygenase encm
UniProt: Q9KHK2
Ligands: FAD, OXY
Pockets: 2 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Putative FAD-dependent oxygenase encm	protein	453	35% helix, 25% strand	Q9KHK2

Ligands and binding sites

FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
OXY · Oxygen molecule · ion · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	680	0.86	0.90	83	FAD, OXY
2	706	0.86	0.89	84	FAD, OXY

Compared structures

6FYC · The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9KHK2
Elsewhere: RCSB PDB 6FYC · PDBe 6FYC · UniProt Q9KHK2

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